| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 10797025 | Biochimica et Biophysica Acta (BBA) - Biomembranes | 2013 | 10 Pages |
Abstract
⺠We present steady-state determinations of reaction intermediates and ATPase activity. ⺠We show occlusion of Rb+ (a K+ congener) during a cycling mode taking place at null [Na+]. ⺠Phosphoenzyme formed by ATP at null [Na+] differs from the one obtained with Na+. ⺠Binding of Na+ to transport sites during catalysis is not at random unless rapid equilibrium holds. ⺠We present a minimal kinetic model that reproduces the results.
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Authors
José L.E. Monti, Mónica R. Montes, Rolando C. Rossi,